Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein
Gustavo P Riboldi1, Hugo Verli, Jeverson Frazzon
1Programa de Pós-Graduação em Biologia Celular e Molecular, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil. riboldi@cbiot.ufrgs.br
BMC Biochemistry
|February 4, 2009
Summary
This study identifies the SUF machinery for iron-sulfur (Fe-S) cluster biosynthesis in Enterococcus faecalis, revealing a unique SufU scaffold protein. Structural analysis highlights flexibility and a novel Gram-positive region, crucial for understanding Fe-S protein maturation in bacteria.
Area of Science:
- Microbiology
- Structural Biology
- Bioinorganic Chemistry
Background:
- Iron-sulfur (Fe-S) clusters are essential prosthetic groups synthesized by complex protein machineries.
- Three systems (NIF, ISC, SUF) are known, but poorly understood in Gram-positive bacteria like Enterococcus spp., emerging pathogens.
- Enterococcus faecalis is a significant cause of nosocomial infections.
Purpose of the Study:
- To perform phylogenetic analysis of the Enterococcus faecalis V583 genome.
- To structurally and conformationally characterize the SufU protein involved in Fe-S cluster biosynthesis.
Main Methods:
- Bioinformatic analysis (BLAST searches) to identify Fe-S cluster biosynthesis genes.
- Phylogenetic analysis to determine evolutionary relationships.
- Molecular dynamics simulations and molecular modeling using crystallographic data (PDB:1su0).
Main Results:
- Identified conserved SUF machinery genes (sufB, sufC, sufD, sufS) and the scaffold protein SufU in Enterococcus spp.
- E. faecalis SufU shares structural similarities with IscU but exhibits unique features, including conserved active site residues.
- Molecular modeling revealed high flexibility in active site regions and a novel 'Gram-positive region' (GPR) in E. faecalis SufU.
Conclusions:
- The SUF machinery is present in Firmicutes, with conserved genes and a SufU scaffold protein (instead of SufA).
- E. faecalis SufU shows structural homology to IscU, indicating conserved functions.
- The identified GPR in E. faecalis SufU may play a role in protein interactions or regulation.
Related Concept Videos
01:57Protein Complexes with Interchangeable Parts
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
01:18Bacterial Gastroenteritis
Bacterial gastroenteritis, characterized by diarrhea, abdominal cramps, and vomiting, is often caused by ingestion of contaminated food or water and is frequently associated with pathogenic Escherichia coli strains. These microbes exploit two principal mechanisms to inflict disease.Shiga toxin–producing E. coli, also referred to as STEC—notably O157:H7—release Shiga toxins that target ribosomes, blocking protein synthesis. The B subunit of the toxin binds the host glycolipid receptor...